biostudies-literatureSchmidt LMMinisterio de Ciencia, Innovación y UniversidadesEMBOGerman Research Councile0049725https://www.ebi.ac.uk/biostudies/studies/S-EPMC12918733biostudies-literatureUnknown208(2)Homologs of the polar landmark proteins HubP and FimV are widespread among bacterial species. They all share several common features, including a periplasmic LysM-like domain, a transmembrane region, an extensive cytoplasmic domain enriched in acidic amino acids, and a C-terminal tetrapeptid-repeat (TPR) domain referred to as the FimV domain. Apart from these conserved general features, however, the proteins exhibit little homology across different bacterial genera. Here, we characterized <i>Pseudomonas putida</i> FimV (<i>Pp</i>FimV) with respect to cellular processes involving FimV or HubP in other species. We found that <i>Pp</i>FimV nonspecifically binds to peptidoglycan via its periplasmic LysM domain, which, together with an immunoglobulin-like domain, is necessary for proper polar pJournal of bacteriologyFunctional characterization of the polar organizer protein FimV in &lt;i&gt;Pseudomonas putida&lt;/i&gt;.PMC12918733TH831 10/1Scientific Exchange Grant 9458PID2021-126121-NB-I00PGC2018-097151-B-I00CEX2020-00108-MLopez-Sanchez AGovantes FSchmidt LMTreuner-Lange AThormann KMPulido-Sanchez MCava FZehner LfalseFunctional characterization of the polar organizer protein FimV in &lt;i&gt;Pseudomonas putida&lt;/i&gt;.Homologs of the polar landmark proteins HubP and FimV are widespread among bacterial species. They all share several common features, including a periplasmic LysM-like domain, a transmembrane region, an extensive cytoplasmic domain enriched in acidic amino acids, and a C-terminal tetrapeptid-repeat (TPR) domain referred to as the FimV domain. Apart from these conserved general features, however, the proteins exhibit little homology across different bacterial genera. Here, we characterized <i>Pseudomonas putida</i> FimV (<i>Pp</i>FimV) with respect to cellular processes involving FimV or HubP in other species. We found that <i>Pp</i>FimV nonspecifically binds to peptidoglycan via its periplasmic LysM domain, which, together with an immunoglobulin-like domain, is necessary for proper polar p2026-01-01T00:00:00Z2026 Feb2026-07-16T09:17:37.774Z2026-07-09T10:46:54.401ZS-EPMC129187334152459410.1128/jb.00497-25